Peptide-directed self-assembly of hydrogels.
This review focuses on the self-assembly of macromolecules mediated by the biorecognition of peptide/protein domains. Structures forming alpha-helices and beta-sheets have been used to mediate self-assembly into hydrogels of peptides, reactive copolymers and peptide motifs, block copolymers, and graft copolymers. Structural factors governing the self-assembly of these molecules into precisely defined three-dimensional structures (hydrogels) are reviewed. The incorporation of peptide motifs into hybrid systems, composed of synthetic and natural macromolecules, enhances design opportunities for new biomaterials when compared to individual components.
Kopecek
Jindrich
J
Department of Pharmaceutics, University of Utah, Salt Lake City, UT 84112, USA. Jindrich.Kopecek@utah.edu
Yang
Jiyuan
J
D001672:Biocompatible Materials / Q000737:chemistry; D020100:Hydrogels / Q000737:chemistry*; D008956:Models, Chemical; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry
D001672:Biocompatible Materials; D020100:Hydrogels; D010455:Peptides; D011108:Polymers; D011506:Proteins